Research workbench
AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (B9E151)
Analyse AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (B9E151) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9E151
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3f713B4B1650176e30B519F2A58Bd9E365E97fD0
- Molecule
- Tryptophan synthase beta chain
- UniProt
- B9E151
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan synthase beta chain | protein | 396 | 47% helix, 19% strand | B9E151 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.81 | 0.97 | 40 | empty |
| 2 | 113 | 0.48 | 0.80 | 15 | empty |
| 3 | 59 | 0.39 | 0.80 | 21 | empty |
| 4 | 65 | 0.32 | 0.75 | 13 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt B9E151
- Elsewhere: UniProt B9E151 · AlphaFold DB B9E151
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